To effectively immobilize an enzyme while maintaining its high activity and stability, the design of supports with controlled geometric structures and heterogeneous surface properties is desirable. Towards this goal, heterogeneous titanium dioxide (TiO₂) surfaces with controlled pore sizes were synthesized in this study and used to efficiently immobilize lipase. The immobilized lipase activity increased by a factor of 1.31 with an increase in the TiO₂ pore size from 11.46 to 21.14 nm. The highest protein loading of 15.52 mg/g was achieved in ethenyl triethoxy silane (ETS)-modified TiO₂ (E-P25) after immobilizing the enzymes at 30 ℃, pH 7.33 for 3 h and using a protein concentration in solution of 0.176 mg/mL. Among the different surface functionalities, the highest activity yield of 428.04 % was accomplished by using TiO₂ calcinated at 650 ℃ and modified by ETS as immobilization support. The immobilized enzymes showed excellent storage stability and retained almost 95 % of their activity after being stored at 4 ℃ for 8 weeks. This research provides experimental evidence that highlights the importance of studying of enzyme immobilization on the supports with synergistically designed geometric structures and surface chemical properties.

为了在保持酶的高活性和稳定性的同时有效地固定酶，需要设计具有受控几何结构和异质表面特性的载体。为了实现这一目标，本研究合成了具有可控孔径的异质二氧化钛 (TiO ₂ ) 表面，并用于有效固定脂肪酶。随着 TiO ₂孔径从 11.46 nm 增加到 21.14 nm ，固定化脂肪酶活性增加了 1.31 倍。在乙烯基三乙氧基硅烷 (ETS) 改性的 TiO _{2 中}实现了 15.52 mg/g 的最高蛋白质负载量(E-P25) 在 30 ℃、pH 7.33 下固定酶 3 小时后，使用蛋白质浓度为 0.176 mg/mL 的溶液。在不同的表面官能度中，以650 ℃煅烧并经ETS改性的TiO ₂为固定载体实现了428.04%的最高活性收率。固定化酶表现出优异的储存稳定性，在 4 ℃下储存 8 周后仍保留了近 95% 的活性。这项研究提供了实验证据，强调了研究酶固定在具有协同设计的几何结构和表面化学性质的载体上的重要性。